Anti-SARS-CoV-2 Nucleocapsid (N) (Clone NP1-B9) – Purified No Carrier Protein
Anti-SARS-CoV-2 Nucleocapsid (N) (Clone NP1-B9) – Purified No Carrier Protein
Product No.: LT7080
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Product No.LT7080 Clone NP1-B9 Target SARS-CoV-2 Nucleocapsid (N) Product Type Recombinant Monoclonal Antibody Alternate Names COV2-NP1-B9, SARS-CoV-2 Nucleocapsid, SARS-CoV-2 Nucleoprotein, Protein N, SARS-CoV N Protein Isotype Human IgG1 Applications ELISA |
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Antibody DetailsProduct DetailsReactive Species SARS-CoV-2 ⋅ Virus Host Species Mouse Expression Host HEK-293 Cells Immunogen SARS-CoV-2 Nucleocapsid (N) Protein Product Concentration ≥1.0 mg/ml Purity ≥90% monomer by analytical SEC and SDS-Page Formulation This recombinant monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration. Product Preparation Recombinant antibodies are manufactured in an animal free facility using only in vitro protein free cell culture techniques and are purified by a multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates. Storage and Handling This antibody may be stored sterile as received at 2-8°C for up to one month. For longer term storage, aseptically aliquot in working volumes without diluting and store at -80°C. Avoid Repeated Freeze Thaw Cycles. Country of Origin USA Shipping Ships Overnight on Blue Ice RRIDAB_2894010 Applications and Recommended Usage? Quality Tested by Leinco ELISA Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change. DescriptionDescriptionSpecificity Anti-SARS-CoV-2 Nucleocapsid, clone NP1-B9, specifically targets an epitope on the SARS-CoV-2 nucleocapsid protein. Futhermore, it is reported to bind to the oligomerization domain of the N protein. Background Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 2019 (COVID-19), is an enveloped, single-stranded, positive-sense RNA virus belonging to the Coronaviridae family1. The SARS-CoV-2 genome encodes four essential proteins: the spike (S), envelope (E), membrane (M), and nucleocapsid (N) proteins2. SARS-CoV-2 shares 79.6% identity with the original SARS-CoV2. The N protein is 46 kDa and consists of two highly conserved structural domains, the N-terminal domain (NTD) and C-terminal domain (CTD), connected by a linker region. The NTD and CTD are involved in a couple of primary functions, including RNA binding and self-oligomerization3,4. This results in binding to and packaging of the viral RNA genome into a helical ribonucleoprotein5. The N protein is involved in other critical steps of the viral life cycle, including transcription, replication, and modulating infected cell signaling pathways6,7. The N protein is a suitable candidate for vaccine development and diagnostic assays8 for several reasons. It is abundantly expressed during infection and is highly conserved, sharing 90% amino acid homology with the SARS-CoV N protein9. Furthermore, antibodies9,10 and memory T cells11,12 targeting the N protein are identified in the sera of convalescent COVID-19 patients, demonstrating it as immunogenic. The N protein also suppresses antiviral RNAi, evading the innate immune system13, suggesting its potential value as a targeted therapeutic. Antigen Distribution The nucleocapsid protein is expressed in the internal nucleocapsid of SARS-CoV-2. NCBI Gene Bank ID Research Area COVID-19 . Infectious Disease . Seasonal and Respiratory Infections . Viral . IVD Raw Material References & Citations1. Zhou, P., Yang, X., Wang, X. et al. Nature 579, 270–273. 2020. 2. Wu, F., Zhao, S., Yu, B. et al. Nature 579, 265–269. 2020. 3. Kang S, Yang M, Hong Z, et al. Acta Pharm Sin B. 10.1016/j.apsb.2020.04.009. 2020. 4. Chang CK, Sue SC, Yu TH, et al. J Biomed Sci. 13(1):59-72. 2006. 5. Hsieh PK, Chang SC, Huang CC, et al. J Virol. 79(22):13848-13855. 2005. 6. Surjit M, Lal SK. Infect Genet Evol. 8(4):397-405. 2008. 7. Hurst KR, Ye R, Goebel SJ, Jayaraman P, Masters PS. J Virol. 84(19):10276-10288. 2010. 8. Liu L, Liu W, Zheng Y, et al. Microbes Infect. 22(4-5):206-211. 2020. 9. Guo L., Ren L., Yang S., et al. Clinical Infectious Diseases: an Official Publication of the Infectious Diseases Society of America. 2020. 10. To K.K., Tsang O.T., Leung W.S., et al. Lancet Infect. Dis. 2020. 11. Grifoni A., Weiskopf D., Ramirez S.I., et al. Cell. 2020. 12. Ni L, Ye F, Cheng ML, et al. Immunity. 52(6):971-977.e3. 2020. 13. Mu J, Xu J, Zhang L, et al. Sci China Life Sci. 1-4. 2020. Technical ProtocolsCertificate of Analysis |
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Products are for research use only. Not for use in diagnostic or therapeutic procedures.